scholarly journals Flavin Oxidoreductase‐Mediated Regeneration of Nicotinamide Adenine Dinucleotide with Dioxygen and Catalytic Amount of Flavin Mononucleotide for One‐Pot Multi‐Enzymatic Preparation of Ursodeoxycholic Acid

2019 ◽  
Author(s):  
Xi Chen ◽  
Yunfeng Cui ◽  
Jinhui Feng ◽  
Yu Wang ◽  
Xiangtao Liu ◽  
...  
Keyword(s):  
Ursodeoxycholic Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Catalytic Amount ◽  
Nicotinamide Adenine ◽  
Flavin Mononucleotide ◽  
Enzymatic Preparation ◽  
One Pot ◽  
Flavin Oxidoreductase

Chemoenzymatic Synthesis of Ubiquitous Biological Redox Cofactors

Synlett ◽  
2017 ◽  
Vol 28 (10) ◽  
pp. 1151-1159 ◽  
Author(s):  
Amnon Kohen ◽  
Priyanka Singh ◽  
Qi Guo
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Enzymatic Synthesis ◽  
Metabolic Enzymes ◽  
Chemoenzymatic Synthesis ◽  
Nicotinamide Adenine ◽  
General Strategy ◽  
One Pot ◽  
Post Translational Modifications ◽  
One Step ◽  
Methylene Tetrahydrofolate

Redox cofactors are utilized by a myriad of proteins, ranging from metabolic enzymes to those performing post-translational modifications. Labeled redox cofactors have served as a vital tool for a broad range of studies. This account describes chemoenzymatic syntheses of the isotopically labeled, biologically important redox cofactors: nicotinamide adenine dinucleotide, methylene tetrahydrofolate, and flavin nucleotides. An overview of the general strategy is presented. These examples demonstrate the utility of enzymatic synthesis.1 Introduction2 Nicotinamide Cofactors2.1 Synthesis of Remote-Labeled 14C-NADPH2.1.1 Synthesis of [Ad-14C]NADPH2.1.2 Synthesis of [Carbonyl-14C]NADPH2.2 Synthesis of S- and R-[4-3H]NADPH2.2.1 One-Step S- and Three-Step R-[4-3H]NADPH Synthesis2.2.2 One-Pot, One-Step R-[4-3H]NADPH Synthesis2.3 Synthesis of S- and R-[Ad-14C, 4-2H]NADPH2.3.1 One-Step S-, Three-Step R-[Ad-14C, 4-2H]NADPH Synthesis2.3.2 One-Pot, One-Step R-[Ad-14C, 4-2H]NADPH Synthesis3 Methylene Tetrahydrofolate4 Flavin Nucleotides5 Conclusions and Outlook

scholarly journals Nicotinamide Adenine Dinucleotide-Dependent Flavin Oxidoreductase of Mycoplasma hyopneumoniae Functions as a Potential Novel Virulence Factor and Not Only as a Metabolic Enzyme

2021 ◽  
Vol 12 ◽  
Author(s):  
Xing Xie ◽  
Fei Hao ◽  
Rong Chen ◽  
Jingjing Wang ◽  
Yanna Wei ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Virulence Factor ◽  
Polyclonal Antibody ◽  
Nicotinamide Adenine Dinucleotide ◽  
Mycoplasma Hyopneumoniae ◽  
Nicotinamide Adenine ◽  
Metabolic Enzyme ◽  
Multiple Sequence ◽  
Enzootic Pneumonia ◽  
Flavin Oxidoreductase

Mycoplasma hyopneumoniae (Mhp) is the main pathogen that causes enzootic pneumonia, a disease that has a significant impact on the pig industry worldwide. The pathogenesis of enzootic pneumonia, especially possible virulence factors of Mhp, has still not been fully elucidated. The transcriptomic and proteomic analyses of different Mhp strains reported in the literature have revealed differences in virulence, and differences in RNA transcription levels between high- and low-virulence strains initially indicated that nicotinamide adenine dinucleotide (NADH)-dependent flavin oxidoreductase (NFOR) was related to Mhp pathogenicity. Prokaryotic expression and purification of the NFOR protein from Mhp were performed, a rabbit-derived polyclonal antibody against NFOR was prepared, and multiple sequence alignment and evolutionary analyses of Mhp NFOR were performed. For the first time, it was found that the NFOR protein was conserved among all Mhp strains, and NFOR was localized to the cell surface and could adhere to immortalized porcine bronchial epithelial cells (hTERT-PBECs). Adhesion to hTERT-PBECs could be specifically inhibited by an anti-NFOR polyclonal antibody, and the rates of adhesion to both high- and low-virulence strains, 168 and 168L, significantly decreased by more than 40%. Moreover, Mhp NFOR not only recognized and interacted with host fibronectin and plasminogen but also induced cellular oxidative stress and apoptosis in hTERT-PBECs. The release of lactate dehydrogenase by hTERT-PBECs incubated with Mhp NFOR was significantly positively correlated with the virulence of Mhp. Overall, in addition to being a metabolic enzyme related to oxidative stress, NFOR may also function as a potential novel virulence factor of Mhp, thus contributing to the pathogenesis of Mhp; these findings provide new ideas and theoretical support for studying the pathogenic mechanisms of other mycoplasmas.

scholarly journals Aerobic oxidation catalyzed by polyoxometalates associated to an artificial reductase at room temperature and in water

2020 ◽  
Vol 7 (12) ◽  
pp. 2362-2369
Author(s):  
Ahmad Naim ◽  
Yoan Chevalier ◽  
Younes Bouzidi ◽  
Priyanka Gairola ◽  
Pierre Mialane ◽  
...  
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Room Temperature ◽  
Aerobic Oxidation ◽  
Nicotinamide Adenine ◽  
Flavin Mononucleotide ◽  
Single Electrons

Four polyoxometalates (POMs) were combined with an artificial reductase based on polyethyleneimine (PEI) and flavin mononucleotide (FMN) which is capable of delivering single electrons upon addition of nicotinamide adenine dinucleotide (NADH).

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